Cathepsin V
Cathepsin V (EC 3.4.22.43, Cathepsin L2, cathepsin U) is an enzyme[1][2][3] that catalyses the following chemical reaction:
| Cathepsin V | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.43 | ||||||||
| CAS number | 223670-00-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
Cathepsin V is a human lysosomal cysteine endopeptidase.
See also
References
- Brömme D, Li Z, Barnes M, Mehler E (February 1999). "Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization". Biochemistry. 38 (8): 2377–85. doi:10.1021/bi982175f. PMID 10029531.
- Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K (September 1998). "Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium". Investigative Ophthalmology & Visual Science. 39 (10): 1789–96. PMID 9727401.
- Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas". Cancer Research. 58 (8): 1624–30. PMID 9563472.
External links
- Cathepsin+V at the US National Library of Medicine Medical Subject Headings (MeSH)
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